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Protein

Versican core protein

Gene

Vcan

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid.

GO - Molecular functioni

GO - Biological processi

  • cell adhesion Source: GO_Central
  • central nervous system development Source: GO_Central
  • glial cell migration Source: MGI
  • heart development Source: MGI
  • osteoblast differentiation Source: MGI
  • regulation of phosphoprotein phosphatase activity Source: MGI
  • skeletal system development Source: GO_Central
  • ureteric bud development Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Hyaluronic acid, Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Versican core protein
Alternative name(s):
Chondroitin sulfate proteoglycan core protein 2
Short name:
Chondroitin sulfate proteoglycan 2
Large fibroblast proteoglycan
PG-M
Gene namesi
Name:Vcan
Synonyms:Cspg2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:102889. Vcan.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: MGI
  • extracellular region Source: MGI
  • extracellular space Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • membrane Source: MGI
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 33573334Versican core proteinPRO_0000017523Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 130By similarity
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence analysis
Disulfide bondi172 ↔ 243By similarity
Disulfide bondi196 ↔ 217By similarity
Disulfide bondi270 ↔ 333By similarity
Disulfide bondi294 ↔ 315By similarity
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence analysis
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence analysis
Glycosylationi441 – 4411N-linked (GlcNAc...)Sequence analysis
Glycosylationi807 – 8071N-linked (GlcNAc...)Sequence analysis
Glycosylationi914 – 9141N-linked (GlcNAc...)Sequence analysis
Glycosylationi951 – 9511N-linked (GlcNAc...)Sequence analysis
Glycosylationi1305 – 13051N-linked (GlcNAc...)Sequence analysis
Glycosylationi1371 – 13711N-linked (GlcNAc...)Sequence analysis
Glycosylationi1678 – 16781N-linked (GlcNAc...)Sequence analysis
Glycosylationi2053 – 20531N-linked (GlcNAc...)Sequence analysis
Glycosylationi2243 – 22431N-linked (GlcNAc...)Sequence analysis
Glycosylationi2361 – 23611N-linked (GlcNAc...)Sequence analysis
Modified residuei2585 – 25851PhosphoserineCombined sources
Modified residuei2586 – 25861PhosphoserineCombined sources
Glycosylationi2626 – 26261N-linked (GlcNAc...)Sequence analysis
Glycosylationi3029 – 30291N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3055 ↔ 3066By similarity
Disulfide bondi3060 ↔ 3075By similarity
Disulfide bondi3077 ↔ 3086By similarity
Disulfide bondi3093 ↔ 3104By similarity
Disulfide bondi3098 ↔ 3113By similarity
Disulfide bondi3115 ↔ 3124By similarity
Disulfide bondi3131 ↔ 3142By similarity
Disulfide bondi3159 ↔ 3251By similarity
Disulfide bondi3227 ↔ 3243By similarity
Disulfide bondi3258 ↔ 3301By similarity
Disulfide bondi3287 ↔ 3314By similarity
Glycosylationi3331 – 33311N-linked (GlcNAc...)Sequence analysis
Glycosylationi3341 – 33411N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylated by FAM20C in the extracellular medium.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

MaxQBiQ62059.
PaxDbiQ62059.
PeptideAtlasiQ62059.
PRIDEiQ62059.

PTM databases

iPTMnetiQ62059.
PhosphoSiteiQ62059.

Expressioni

Tissue specificityi

Isoform V2 is found only in brain.

Developmental stagei

Disappears after the cartilage development.

Gene expression databases

CleanExiMM_VCAN.

Interactioni

Subunit structurei

Interacts with FBLN1.1 Publication

GO - Molecular functioni

  • protein phosphatase binding Source: MGI

Protein-protein interaction databases

IntActiQ62059. 2 interactions.
MINTiMINT-4092234.
STRINGi10090.ENSMUSP00000105173.

Structurei

3D structure databases

ProteinModelPortaliQ62059.
SMRiQ62059. Positions 3129-3254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 146123Ig-like V-typeAdd
BLAST
Domaini150 – 24596Link 1PROSITE-ProRule annotationAdd
BLAST
Domaini251 – 34797Link 2PROSITE-ProRule annotationAdd
BLAST
Domaini3051 – 308737EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini3089 – 312537EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini3138 – 3252115C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini3256 – 331661SushiPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni348 – 1308961GAG-alpha (glucosaminoglycan attachment domain)Add
BLAST
Regioni1309 – 30511743GAG-betaAdd
BLAST

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 2 Link domains.PROSITE-ProRule annotation
Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Immunoglobulin domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiENOG410IFXS. Eukaryota.
ENOG410ZPDG. LUCA.
HOGENOMiHOG000168523.
HOVERGENiHBG051140.
InParanoidiQ62059.
PhylomeDBiQ62059.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 3 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link_dom.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 2 hits.
[Graphical view]
PRINTSiPR01265. LINKMODULE.
SMARTiSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF56436. SSF56436. 3 hits.
SSF57535. SSF57535. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50835. IG_LIKE. 1 hit.
PS01241. LINK_1. 2 hits.
PS50963. LINK_2. 2 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform V0 (identifier: Q62059-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLINMKGILW MCSTLLLTHA LHQAKMETSP PVKGSLSGKV VLPCHFSTLP
60 70 80 90 100
TLPPNYNTSE FLRIKWSKME VDKNGKDIKE TTVLVAQNGN IKIGQDYKGR
110 120 130 140 150
VSVPTHPDDV GDASLTMVKL RASDAAVYRC DVMYGIEDTQ DTMSLAVDGV
160 170 180 190 200
VFHYRAATSR YTLNFAAAQQ ACLDIGAVIA SPEQLFAAYE DGFEQCDAGW
210 220 230 240 250
LSDQTVRYPI RAPREGCYGD MMGKEGVRTY GFRSPQETYD VYCYVDHLDG
260 270 280 290 300
DVFHITAPSK FTFEEAEAEC TSRDARLATV GELQAAWRNG FDQCDYGWLS
310 320 330 340 350
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTCFPLPDSR FDAYCFKPKQ
360 370 380 390 400
NISEATTIEM NILAETSSPS LSKEPHMVPD RATPVIPLAT ELPIFTTHFP
410 420 430 440 450
PAGNIVNSEQ KSVVYSQAIT GRLATESPTT TRNTINSWDL NDSLASGSGP
460 470 480 490 500
LGMPDISEIK EEELRSTTVI SQHATGSQAV ITEDTQTHES VSQIEQIEVG
510 520 530 540 550
PLVTSMEITN HISLKELPEK NKTPYESTEV TLEHTTEMPT VSASPELATT
560 570 580 590 600
SHYGFTLRED DREDRTLTVR SDQSTRVFSQ IPEVITVSKT SEDTTYSQLG
610 620 630 640 650
DLESISTSTI TMLGTDRSLI DKEKEPKTNG KVTEDEFGQS QPTTTFPSQH
660 670 680 690 700
LTEVELLPYS GDTTSVEGIS TVIYPSLQTD VTQGRERTET PRPELKKDPY
710 720 730 740 750
TVDEIPEKVT KDPFIGKTEE VFSGMPLSTS SSESSVERTE SVSPALTIEK
760 770 780 790 800
LTGKPTEARD VEEMTTLTRL ETDVTKSDKD VTRVHLTHST LNVEVVTVSK
810 820 830 840 850
WPGDEDNSTS KPLPSTEHAG FTKLPPVPLS TIGINGKDKE IPSFTDGGGE
860 870 880 890 900
YTLFPDGTPK PLEKVSEEDL ASGELTVTFH TSTSIGSAEK SASGEPTTGD
910 920 930 940 950
RFLPTTSTED QVINATAEGS ALGEDTEASK PLFTGPPFVH TSDVEELAFV
960 970 980 990 1000
NYSSTQEPTT YVDISHTSPL SIIPKTEWSV LETSVPLEDE ILGKSDQDIL
1010 1020 1030 1040 1050
EQTHLEATMS PGALRTTGVS QGETQEEPQT PGSPFPTFSS TAVMAKETTA
1060 1070 1080 1090 1100
FEEGEGSTYT PSEGRLMTGS ERVPGLETTP VGTSYPPGAI TDQEVEMDTM
1110 1120 1130 1140 1150
VTLMSTIRPT VVSSTESEVI YEAEGSSPTE FASTLRPFQT HVTQLMEETT
1160 1170 1180 1190 1200
EEGKKASLDY TDLGSGLFEP RATELPKFPS TPSDISVFTA IDSLHRTPPL
1210 1220 1230 1240 1250
SPSSSFTEEQ RVFEEESSEK TTGDILPGES VTQHPVTTLI DIVAMKTESD
1260 1270 1280 1290 1300
IDHMTSKPPV TQPTRPSVVE RKTTSKTQEL STSTPAAGTK FHPDINVYII
1310 1320 1330 1340 1350
EVRENKTGRL SDMIVSGHPI DSESKEEEPC SEETDPLHDL FAEILPELPD
1360 1370 1380 1390 1400
SFEIDIYHSE EDEDGEEDCV NATDVTTTPS VQYINGKQLV TTVPKDPEAA
1410 1420 1430 1440 1450
EARRGQYESV APSQNFPDSS ATDTHQFILA ETESSTTMQF KKSKEGTELL
1460 1470 1480 1490 1500
EITWKPETYP ETPDHVSSGE PDVFPTLSSH DGKTTRWSES ITESSPNLEN
1510 1520 1530 1540 1550
PVHKQPKPVP LFPEESSGEG AIEQASQETI LSRATEVALG KETDQSPTLS
1560 1570 1580 1590 1600
TSSILSSSVS VNVLEEEPLT LTGISQTDES MSTIESWVEI TPSQTVKFSE
1610 1620 1630 1640 1650
SSSAPIIEGS GEVEENKNKI FNMVTDLPQR DPTDTLSPLD MSKIMITNHH
1660 1670 1680 1690 1700
IYIPATIAPL DSKLPSPDAR PTTVWNSNST SEWVSDKSFE GRKKKENEDE
1710 1720 1730 1740 1750
EGAVNAAHQG EVRAATERSD HLLLTPELES SNVDASSDLA TWEGFILETT
1760 1770 1780 1790 1800
PTESEKEMAN STPVFRETIG VANVEAQPFE HSSSSHPRVQ EELTTLSGNP
1810 1820 1830 1840 1850
PSLFTDLGSG DASTGMELIT ASLFTLDLES ETKVKKELPS TPSPSVEISS
1860 1870 1880 1890 1900
SFEPTGLTPS TVLDIEIAGV MSQTSQKTLI SEISGKPTSQ SGVRDLYTGF
1910 1920 1930 1940 1950
PMGEDFSGDF SEYPTVSYPT MKEETVGMGG SDDERVRDTQ TSSSIPTTSD
1960 1970 1980 1990 2000
NIYPVPDSKG PDSTVASTTA FPWEEVMSSA EGSGEQLASV RSSVGPVLPL
2010 2020 2030 2040 2050
AVDIFSGTES PYFDEEFEEV AAVTEANERP TVLPTAASGN TVDLTENGYI
2060 2070 2080 2090 2100
EVNSTMSLDF PQTMEPSKLW SKPEVNLDKQ EIGRETVTKE KAQGQKTFES
2110 2120 2130 2140 2150
LHSSFAPEQT ILETQSLIET EFQTSDYSML TTLKTYITNK EVEEEGMSIA
2160 2170 2180 2190 2200
HMSTPGPGIK DLESYTTHPE APGKSHSFSA TALVTESGAA RSVLMDSSTQ
2210 2220 2230 2240 2250
EEESIKLFQK GVKLTNKESN ADLSFSGLGS GGALPPLPTT SVNLTDMKQI
2260 2270 2280 2290 2300
ISTLYAETSH MESLGTSILG DKMEDHERME DVSSNEVRML ISKIGSISQD
2310 2320 2330 2340 2350
STEALDTTLS HTGTEEPTTS TLPFVKLMDL ERSPKQDPSG GKRKPKTHRP
2360 2370 2380 2390 2400
QTMSGLISNE NSSASEAEEG ATSPTAFLPQ TYSVEMTKHF APSESQPSDL
2410 2420 2430 2440 2450
FNVNSGEGSG EVDTLDLVYT SGTTQASSQG DSMLASHGFL EKHPEVSKTE
2460 2470 2480 2490 2500
AGATDVSPTA SAMFLHHSEY KSSLYPTSTL PSTEPYKSPS EGIEDGLQDN
2510 2520 2530 2540 2550
IQFEGSTLKP SRRKTTESII IDLDKEDSKD LGLTITESAI VKSLPELTSD
2560 2570 2580 2590 2600
KNIIIDIDHT KPVYEYIPGI QTDLDPEIKL ESHGSSEESL QVQEKYEGAV
2610 2620 2630 2640 2650
TLSPTEESFE GSGDALLAGY TQAIYNESVT PNDGKQAEDI SFSFATGIPV
2660 2670 2680 2690 2700
SSTETELHTF FPTASTLHIP SKLTTASPEI DKPNIEAISL DDIFESSTLS
2710 2720 2730 2740 2750
DGQAIADQSE VISTLGHLEK TQEEYEEKKY GGPSFQPEFF SGVGEVLTDP
2760 2770 2780 2790 2800
PAYVSIGSTY LIAQTLTELP NVVRPSDSTH YTEATPEVSS LAELSPQIPS
2810 2820 2830 2840 2850
SPFPVYVDNG VSKFPEVPHT SAQPVSTVTS SQKSIESPFK EVHANIEETI
2860 2870 2880 2890 2900
KPLGGNVHRT EPPSMSRDPA LDVSEDESKH KLLEELETSP TKPETSQDFP
2910 2920 2930 2940 2950
NKAKDHIPGE TVGMLAGIRT TESEPVITAD DMELGGATQQ PHSASAAFRV
2960 2970 2980 2990 3000
ETGMVPQPIQ QEPERPTFPS LEINHETHTS LFGESILATS EKQVSQKILD
3010 3020 3030 3040 3050
NSNQATVSST LDLHTAHALS PFSILDNSNE TAFLIGISEE SVEGTAVYLP
3060 3070 3080 3090 3100
GPDLCKTNPC LNGGTCYPTE TSYVCTCAPG YSGDQCELDF DECHSNPCRN
3110 3120 3130 3140 3150
GATCVDGFNT FRCLCLPSYV GALCEQDTET CDYGWHKFQG QCYKYFAHRR
3160 3170 3180 3190 3200
TWDAAERECR LQGAHLTSIL SHEEQMFVNR VGHDYQWIGL NDKMFEHDFR
3210 3220 3230 3240 3250
WTDGSALQYE NWRPNQPDSF FSAGEDCVVI IWHENGQWND VPCNYHLTYT
3260 3270 3280 3290 3300
CKKGTVACGQ PPVVENAKTF GKMKPRYEIN SLIRYHCKDG FIQRHLPTIR
3310 3320 3330 3340 3350
CLGNGRWAMP KITCMNPSAY QRTYSKKYLK NSSSAKDNSI NTSKHEHRWS

RRQETRR
Length:3,357
Mass (Da):366,787
Last modified:June 13, 2006 - v2
Checksum:iAE82A0D942B8323A
GO
Isoform V1 (identifier: Q62059-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     348-348: P → R
     349-1308: Missing.

Show »
Length:2,397
Mass (Da):262,705
Checksum:i07CB2047C10A2226
GO
Isoform V2 (identifier: Q62059-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1309-3051: Missing.

Show »
Length:1,614
Mass (Da):178,258
Checksum:iD1B5E6E19671DC56
GO
Isoform V3 (identifier: Q62059-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     348-348: P → R
     349-3051: Missing.

Show »
Length:654
Mass (Da):74,177
Checksum:iA996C1142D8FCD16
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1261A → G (PubMed:16141072).Curated
Sequence conflicti1657 – 16571I → T (PubMed:16141072).Curated
Sequence conflicti1673 – 16797TVWNSNS → QFGIQTA (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei348 – 3481P → R in isoform V1 and isoform V3. 3 PublicationsVSP_003087
Alternative sequencei349 – 30512703Missing in isoform V3. 1 PublicationVSP_003090Add
BLAST
Alternative sequencei349 – 1308960Missing in isoform V1. 2 PublicationsVSP_003088Add
BLAST
Alternative sequencei1309 – 30511743Missing in isoform V2. 1 PublicationVSP_003089Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16263 mRNA. Translation: BAA03796.1.
D28599 mRNA. No translation available.
D32040 mRNA. Translation: BAA06802.1.
AK014525 mRNA. Translation: BAB29411.3.
PIRiA55535.
UniGeneiMm.158700.
Mm.410783.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Versican

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16263 mRNA. Translation: BAA03796.1.
D28599 mRNA. No translation available.
D32040 mRNA. Translation: BAA06802.1.
AK014525 mRNA. Translation: BAB29411.3.
PIRiA55535.
UniGeneiMm.158700.
Mm.410783.

3D structure databases

ProteinModelPortaliQ62059.
SMRiQ62059. Positions 3129-3254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ62059. 2 interactions.
MINTiMINT-4092234.
STRINGi10090.ENSMUSP00000105173.

PTM databases

iPTMnetiQ62059.
PhosphoSiteiQ62059.

Proteomic databases

MaxQBiQ62059.
PaxDbiQ62059.
PeptideAtlasiQ62059.
PRIDEiQ62059.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:102889. Vcan.

Phylogenomic databases

eggNOGiENOG410IFXS. Eukaryota.
ENOG410ZPDG. LUCA.
HOGENOMiHOG000168523.
HOVERGENiHBG051140.
InParanoidiQ62059.
PhylomeDBiQ62059.

Miscellaneous databases

PROiQ62059.
SOURCEiSearch...

Gene expression databases

CleanExiMM_VCAN.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 3 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link_dom.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 2 hits.
[Graphical view]
PRINTSiPR01265. LINKMODULE.
SMARTiSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF56436. SSF56436. 3 hits.
SSF57535. SSF57535. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50835. IG_LIKE. 1 hit.
PS01241. LINK_1. 2 hits.
PS50963. LINK_2. 2 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple forms of mouse PG-M, a large chondroitin sulfate proteoglycan generated by alternative splicing."
    Ito K., Shinomura T., Zako M., Ujita M., Kimata K.
    J. Biol. Chem. 270:958-965(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V0; V1 AND V2).
    Strain: C57BL/6J and Swiss Webster.
    Tissue: Brain and Endothelial cell.
  2. "Expression of PG-M(V3), an alternatively spliced form of PG-M without a chondroitin sulfate attachment in region in mouse and human tissues."
    Zako M., Shinomura T., Ujita M., Ito K., Kimata K.
    J. Biol. Chem. 270:3914-3918(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V3).
    Strain: C57BL/6J.
    Tissue: Endothelial cell.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1691 (ISOFORM V1).
    Strain: C57BL/6J.
    Tissue: Skin.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 277-288, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican."
    Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.
    J. Biol. Chem. 274:20444-20449(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBLN1.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2585 AND SER-2586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung and Spleen.

Entry informationi

Entry nameiCSPG2_MOUSE
AccessioniPrimary (citable) accession number: Q62059
Secondary accession number(s): Q62058, Q9CUU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 13, 2006
Last modified: July 6, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.